RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/12524439http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12524439http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12524439http://www.w3.org/2000/01/rdf-schema#comment"Akt (also called protein kinase B) is one of the major downstream targets of the phosphatidylinositol 3-kinase pathway. This protein kinase has been implicated in insulin signaling, stimulation of cellular growth, and inhibition of apoptosis as well as transformation of cells. Although a number of cellular proteins have been identified as putative targets of the enzyme, additional substrates may play a role in the varied responses elicited by this enzyme. We have used a combination of 14-3-3 binding and recognition by an antibody to the phosphorylation consensus of the enzyme to identify and isolate one of the major substrates of Akt, which is also a 14-3-3 binding protein. This 40-kDa protein, designated PRAS40, is a proline-rich Akt substrate. Demonstration that it is a substrate of Akt was accomplished by showing that 1) PRAS40 was phosphorylated in vitro by purified Akt on the same site that was phosphorylated in insulin-treated cells; 2) activation of an inducible Akt was alone sufficient to stimulate the phosphorylation of PRAS40; and 3) cells lacking Akt1 and Akt2 exhibit a diminished ability to phosphorylate this protein. Thus, PRAS40 is a novel substrate of Akt, the phosphorylation of which leads to the binding of this protein to 14-3-3."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m210837200"xsd:string
http://purl.uniprot.org/citations/12524439http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m210837200"xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Bae S.S."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Bae S.S."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Birnbaum M.J."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Birnbaum M.J."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Schaefer E."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Schaefer E."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Guzzetta A.W."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Guzzetta A.W."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Kovacina K.S."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Kovacina K.S."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Park G.Y."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Park G.Y."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Roth R.A."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/author"Roth R.A."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/pages"10189-10194"xsd:string
http://purl.uniprot.org/citations/12524439http://purl.uniprot.org/core/pages"10189-10194"xsd:string